2022 - Research.com Chemistry in Russia Leader Award
His primary areas of investigation include Biochemistry, Butyrylcholinesterase, Enzyme, Acetylcholinesterase and Stereochemistry. His study connects Function and Biochemistry. His Butyrylcholinesterase research includes elements of Cholinesterase, Echothiophate, Paraoxon, Organophosphate and Catalysis.
His work on Butyrylthiocholine and Substrate as part of general Enzyme research is often related to Lactonase, thus linking different fields of science. Particularly relevant to Nerve agent is his body of work in Acetylcholinesterase. The Stereochemistry study combines topics in areas such as Tabun, Oxime, Bond cleavage and Active site.
The scientist’s investigation covers issues in Butyrylcholinesterase, Biochemistry, Stereochemistry, Enzyme and Acetylcholinesterase. His research on Butyrylcholinesterase also deals with topics like
He works mostly in the field of Stereochemistry, limiting it down to concerns involving Active site and, occasionally, Serine. His work on Catalysis expands to the thematically related Enzyme. The various areas that he examines in his Acetylcholinesterase study include Organophosphate poisoning, Myasthenia gravis and Pharmacology.
Patrick Masson spends much of his time researching Butyrylcholinesterase, Acetylcholinesterase, Biochemistry, Enzyme and Nerve agent. Patrick Masson interconnects Recombinant DNA, Butyrylthiocholine, Chromatography, Stereochemistry and Peptide in the investigation of issues within Butyrylcholinesterase. Patrick Masson combines subjects such as Myasthenia gravis, Organophosphate poisoning and Pharmacology, Cholinesterase with his study of Acetylcholinesterase.
In his study, Antibody is inextricably linked to Molecular biology, which falls within the broad field of Biochemistry. A large part of his Enzyme studies is devoted to Substrate. The study incorporates disciplines such as Toxicology, Catalysis and Detoxification in addition to Nerve agent.
His main research concerns Butyrylcholinesterase, Biochemistry, Enzyme, Acetylcholinesterase and Nerve agent. His Butyrylcholinesterase study combines topics in areas such as Cholinesterase, Stereochemistry, Phosphate, Tetramer and Peptide. His biological study spans a wide range of topics, including Anti-idiotypic antibodies and Neutralization.
His work on Catalytic triad as part of general Enzyme research is frequently linked to Human decontamination, thereby connecting diverse disciplines of science. His Acetylcholinesterase research is multidisciplinary, relying on both Plasma protein binding, Pharmacology, Neuroprotection, Hydrolase and Active site. His study in Nerve agent is interdisciplinary in nature, drawing from both Organophosphate poisoning, Catalysis and Detoxification.
This overview was generated by a machine learning system which analysed the scientist’s body of work. If you have any feedback, you can contact us here.
High Pressure Effects on Protein Structure and Function
Vadim V. Mozhaev;Karel Heremans;Johannes Frank;Patrick Masson.
Proteins (1996)
Crystal structure of human butyrylcholinesterase and of its complexes with substrate and products.
Yvain Nicolet;Oksana Lockridge;Patrick Masson;Juan C. Fontecilla-Camps.
Journal of Biological Chemistry (2003)
The Arabidopsis thaliana AGRAVITROPIC 1 gene encodes a component of the polar-auxin-transport efflux carrier
Rujin Chen;Pierre Hilson;John Sedbrook;Elizabeth Rosen.
Proceedings of the National Academy of Sciences of the United States of America (1998)
Butyrylcholinesterase, paraoxonase, and albumin esterase, but not carboxylesterase, are present in human plasma
Bin Li;Meghan Sedlacek;Indumathi Manoharan;Rathnam Boopathy.
Biochemical Pharmacology (2005)
Effects of high pressure on proteins
Claude Balny;Patrick Masson.
Food Reviews International (1993)
Exploiting the effects of high hydrostatic pressure in biotechnological applications
Vadim V. Mozhaev;Vadim V. Mozhaev;Karel Heremans;Johannes Frank;Patrick Masson.
Trends in Biotechnology (1994)
High pressure effects on biological macromolecules: from structural changes to alteration of cellular processes.
Claude Balny;Patrick Masson;Karel Heremans.
Biochimica et Biophysica Acta (2002)
Butyrylcholinesterase for protection from organophosphorus poisons; catalytic complexities and hysteretic behavior
Patrick Masson;Oksana Lockridge.
Archives of Biochemistry and Biophysics (2010)
A single amino acid substitution, Gly117His, confers phosphotriesterase (organophosphorus acid anhydride hydrolase) activity on human butyrylcholinesterase
Oksana Lockridge;Renee M. Blong;Patrick Masson;Marie Thérèse Froment.
Biochemistry (1997)
Pesticides and susceptible populations: people with butyrylcholinesterase genetic variants may be at risk.
O Lockridge;P Masson.
Neurotoxicology (2000)
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